Abstract
T-CELL accessory molecules, particularly CD4 and CD8, seem to be involved in the control of T-cell activation by antigen. Precisely how such molecules operate is not fully understood, but evidence to date suggests a dual role, as receptors binding ligands on stimulator cells1,2 and by direct or indirect involvement in intracellular signalling events3–5. In mouse, truncated 'tailless' CD8 molecules occur naturally (CD8α′ polypeptides) and although they are expressed on the surface of thymocytes, they are not expressed on the surface of mature T cells6. In this study, we show that truncated CD8 molecules are impaired in their ability to interact with the protein tyrosine kinase, p56lck, and have decreased ability to restore immune responsiveness in vitro. Our data support a dual function for CD8 molecules correlated with expression of external domains and cytoplasmic domains, respectively. Both functions appear to be critical for a competent immune system in vivo.
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Zamoyska, R., Derham, P., Gorman, S. et al. Inability of CD8α′polypeptides to associate with p56lck correlates with impaired function in vitro and lack of expression in vivo. Nature 342, 278–281 (1989). https://doi.org/10.1038/342278a0
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DOI: https://doi.org/10.1038/342278a0
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